2gpw
From Proteopedia
(New page: 200px<br /><applet load="2gpw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gpw, resolution 2.20Å" /> '''Crystal Structure of...) |
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| - | [[Image:2gpw.gif|left|200px]]<br /><applet load="2gpw" size=" | + | [[Image:2gpw.gif|left|200px]]<br /><applet load="2gpw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2gpw, resolution 2.20Å" /> | caption="2gpw, resolution 2.20Å" /> | ||
'''Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.'''<br /> | '''Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Acetyl-coenzyme A carboxylases (ACCs) have crucial roles in fatty acid | + | Acetyl-coenzyme A carboxylases (ACCs) have crucial roles in fatty acid metabolism. The biotin carboxylase (BC) subunit of Escherichia coli ACC is believed to be active only as a dimer, although the crystal structure shows that the active site of each monomer is 25 A from the dimer interface. We report here biochemical, biophysical, and structural characterizations of BC carrying single-site mutations in the dimer interface. Our studies demonstrate that two of the mutants, R19E and E23R, are monomeric in solution but have only a 3-fold loss in catalytic activity. The crystal structures of the E23R and F363A mutants show that they can still form the correct dimer at high concentrations. Our data suggest that dimerization is not an absolute requirement for the catalytic activity of the E. coli BC subunit, and we propose a new model for the molecular mechanism of action for BC in multisubunit and multidomain ACCs. |
==About this Structure== | ==About this Structure== | ||
| - | 2GPW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Biotin_carboxylase Biotin carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.14 6.3.4.14] Full crystallographic information is available from [http:// | + | 2GPW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Biotin_carboxylase Biotin carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.14 6.3.4.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GPW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chang, G | + | [[Category: Chang, G G.]] |
| - | [[Category: Chou, C | + | [[Category: Chou, C Y.]] |
[[Category: Shen, Y.]] | [[Category: Shen, Y.]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
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[[Category: fatty acid synthesis]] | [[Category: fatty acid synthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:34:04 2008'' |
Revision as of 15:34, 21 February 2008
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Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.
Overview
Acetyl-coenzyme A carboxylases (ACCs) have crucial roles in fatty acid metabolism. The biotin carboxylase (BC) subunit of Escherichia coli ACC is believed to be active only as a dimer, although the crystal structure shows that the active site of each monomer is 25 A from the dimer interface. We report here biochemical, biophysical, and structural characterizations of BC carrying single-site mutations in the dimer interface. Our studies demonstrate that two of the mutants, R19E and E23R, are monomeric in solution but have only a 3-fold loss in catalytic activity. The crystal structures of the E23R and F363A mutants show that they can still form the correct dimer at high concentrations. Our data suggest that dimerization is not an absolute requirement for the catalytic activity of the E. coli BC subunit, and we propose a new model for the molecular mechanism of action for BC in multisubunit and multidomain ACCs.
About this Structure
2GPW is a Single protein structure of sequence from Escherichia coli. Active as Biotin carboxylase, with EC number 6.3.4.14 Full crystallographic information is available from OCA.
Reference
Is dimerization required for the catalytic activity of bacterial biotin carboxylase?, Shen Y, Chou CY, Chang GG, Tong L, Mol Cell. 2006 Jun 23;22(6):807-18. PMID:16793549
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